BOLA1_HUMAN
ID BOLA1_HUMAN Reviewed; 137 AA.
AC Q9Y3E2; B2R7K2; D3DUZ4; Q5QNY0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=BolA-like protein 1 {ECO:0000305};
DE AltName: Full=hBolA {ECO:0000303|PubMed:18548201};
GN Name=BOLA1 {ECO:0000312|HGNC:HGNC:24263};
GN ORFNames=CGI-143 {ECO:0000303|PubMed:10810093};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=18548201; DOI=10.1007/s11010-008-9809-2;
RA Zhou Y.B., Cao J.B., Wan B.B., Wang X.R., Ding G.H., Zhu H., Yang H.M.,
RA Wang K.S., Zhang X., Han Z.G.;
RT "hBolA, novel non-classical secreted proteins, belonging to different BolA
RT family with functional divergence.";
RL Mol. Cell. Biochem. 317:61-68(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GLRX5.
RX PubMed=22746225; DOI=10.1089/ars.2011.4253;
RA Willems P., Wanschers B.F., Esseling J., Szklarczyk R., Kudla U.,
RA Duarte I., Forkink M., Nooteboom M., Swarts H., Gloerich J., Nijtmans L.,
RA Koopman W., Huynen M.A.;
RT "BOLA1 is an aerobic protein that prevents mitochondrial morphology changes
RT induced by glutathione depletion.";
RL Antioxid. Redox Signal. 18:129-138(2013).
RN [9]
RP INTERACTION WITH GLRX5.
RX PubMed=27532773; DOI=10.7554/elife.15991;
RA Melber A., Na U., Vashisht A., Weiler B.D., Lill R., Wohlschlegel J.A.,
RA Winge D.R.;
RT "Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial
RT clients.";
RL Elife 5:0-0(2016).
RN [10] {ECO:0007744|PDB:5LCI}
RP STRUCTURE BY NMR OF 21-137, AND INTERACTION WITH GLRX5.
RX PubMed=27532772; DOI=10.7554/elife.16673;
RA Uzarska M.A., Nasta V., Weiler B.D., Spantgar F., Ciofi-Baffoni S.,
RA Saviello M.R., Gonnelli L., Muehlenhoff U., Banci L., Lill R.;
RT "Mitochondrial Bol1 and Bol3 function as assembly factors for specific
RT iron-sulfur proteins.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Acts as a mitochondrial iron-sulfur (Fe-S) cluster assembly
CC factor that facilitates (Fe-S) cluster insertion into a subset of
CC mitochondrial proteins (By similarity). Probably acts together with the
CC monothiol glutaredoxin GLRX5 (PubMed:27532772). May protect cells
CC against oxidative stress (PubMed:22746225).
CC {ECO:0000250|UniProtKB:Q3E793, ECO:0000269|PubMed:22746225,
CC ECO:0000305|PubMed:27532772}.
CC -!- SUBUNIT: Interacts with GLRX5 (PubMed:22746225, PubMed:27532773,
CC PubMed:27532772). {ECO:0000269|PubMed:22746225,
CC ECO:0000269|PubMed:27532772, ECO:0000269|PubMed:27532773}.
CC -!- INTERACTION:
CC Q9Y3E2; Q13490: BIRC2; NbExp=7; IntAct=EBI-1049556, EBI-514538;
CC Q9Y3E2; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-1049556, EBI-517623;
CC Q9Y3E2; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-1049556, EBI-946029;
CC Q9Y3E2; O76003: GLRX3; NbExp=14; IntAct=EBI-1049556, EBI-374781;
CC Q9Y3E2; PRO_0000141650 [Q86SX6]: GLRX5; NbExp=6; IntAct=EBI-1049556, EBI-27823755;
CC Q9Y3E2; Q7Z353: HDX; NbExp=3; IntAct=EBI-1049556, EBI-1052734;
CC Q9Y3E2; Q9UMS0: NFU1; NbExp=2; IntAct=EBI-1049556, EBI-725252;
CC Q9Y3E2; Q6F5E7: TXNRD3NB; NbExp=3; IntAct=EBI-1049556, EBI-18122152;
CC Q9Y3E2; P98170: XIAP; NbExp=3; IntAct=EBI-1049556, EBI-517127;
CC Q9Y3E2; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-1049556, EBI-10172590;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22746225}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18548201}.
CC -!- SIMILARITY: Belongs to the BolA/IbaG family. {ECO:0000305}.
CC -!- CAUTION: Was initially reported to be secreted via a non-classical
CC export pathway (PubMed:18548201). It was however later shown that it
CC localizes to mitochondria, in agreement with other members of the
CC family (PubMed:22746225). {ECO:0000269|PubMed:18548201,
CC ECO:0000269|PubMed:22746225}.
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DR EMBL; AF151901; AAD34138.1; -; mRNA.
DR EMBL; AK313014; BAG35849.1; -; mRNA.
DR EMBL; AL591493; CAI12571.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53599.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53600.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53601.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53602.1; -; Genomic_DNA.
DR EMBL; BC063405; AAH63405.1; -; mRNA.
DR CCDS; CCDS939.1; -.
DR RefSeq; NP_001307954.1; NM_001321025.1.
DR RefSeq; NP_001307955.1; NM_001321026.1.
DR RefSeq; NP_057158.1; NM_016074.4.
DR RefSeq; XP_006711411.1; XM_006711348.3.
DR PDB; 5LCI; NMR; -; A=21-137.
DR PDBsum; 5LCI; -.
DR AlphaFoldDB; Q9Y3E2; -.
DR SMR; Q9Y3E2; -.
DR BioGRID; 119233; 34.
DR ComplexPortal; CPX-6862; Mitochondrial BOLA1-GLRX5 iron-sulfur cluster assembly complex.
DR IntAct; Q9Y3E2; 34.
DR MINT; Q9Y3E2; -.
DR STRING; 9606.ENSP00000358149; -.
DR iPTMnet; Q9Y3E2; -.
DR PhosphoSitePlus; Q9Y3E2; -.
DR BioMuta; BOLA1; -.
DR DMDM; 8134821; -.
DR EPD; Q9Y3E2; -.
DR jPOST; Q9Y3E2; -.
DR MassIVE; Q9Y3E2; -.
DR MaxQB; Q9Y3E2; -.
DR PaxDb; Q9Y3E2; -.
DR PeptideAtlas; Q9Y3E2; -.
DR PRIDE; Q9Y3E2; -.
DR ProteomicsDB; 86029; -.
DR Antibodypedia; 1825; 181 antibodies from 26 providers.
DR DNASU; 51027; -.
DR Ensembl; ENST00000369150.1; ENSP00000358146.1; ENSG00000178096.9.
DR Ensembl; ENST00000369152.6; ENSP00000358148.5; ENSG00000178096.9.
DR Ensembl; ENST00000369153.2; ENSP00000358149.1; ENSG00000178096.9.
DR GeneID; 51027; -.
DR KEGG; hsa:51027; -.
DR MANE-Select; ENST00000369152.6; ENSP00000358148.5; NM_016074.5; NP_057158.1.
DR UCSC; uc001etf.4; human.
DR CTD; 51027; -.
DR GeneCards; BOLA1; -.
DR HGNC; HGNC:24263; BOLA1.
DR HPA; ENSG00000178096; Low tissue specificity.
DR MIM; 613181; gene.
DR neXtProt; NX_Q9Y3E2; -.
DR OpenTargets; ENSG00000178096; -.
DR PharmGKB; PA142672552; -.
DR VEuPathDB; HostDB:ENSG00000178096; -.
DR eggNOG; KOG2313; Eukaryota.
DR GeneTree; ENSGT00510000048165; -.
DR HOGENOM; CLU_109462_3_0_1; -.
DR InParanoid; Q9Y3E2; -.
DR OMA; CLGGFGK; -.
DR OrthoDB; 1603661at2759; -.
DR PhylomeDB; Q9Y3E2; -.
DR TreeFam; TF354266; -.
DR PathwayCommons; Q9Y3E2; -.
DR SignaLink; Q9Y3E2; -.
DR BioGRID-ORCS; 51027; 6 hits in 1067 CRISPR screens.
DR GenomeRNAi; 51027; -.
DR Pharos; Q9Y3E2; Tbio.
DR PRO; PR:Q9Y3E2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y3E2; protein.
DR Bgee; ENSG00000178096; Expressed in apex of heart and 116 other tissues.
DR Genevisible; Q9Y3E2; HS.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IC:ComplexPortal.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IC:ComplexPortal.
DR Gene3D; 3.30.300.90; -; 1.
DR InterPro; IPR002634; BolA.
DR InterPro; IPR036065; BolA-like_sf.
DR Pfam; PF01722; BolA; 1.
DR SUPFAM; SSF82657; SSF82657; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Phosphoprotein; Reference proteome.
FT CHAIN 1..137
FT /note="BolA-like protein 1"
FT /id="PRO_0000201233"
FT REGION 114..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D8S9"
FT VARIANT 98
FT /note="G -> A (in dbSNP:rs1044808)"
FT /id="VAR_033630"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:5LCI"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:5LCI"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5LCI"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:5LCI"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:5LCI"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:5LCI"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:5LCI"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:5LCI"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:5LCI"
SQ SEQUENCE 137 AA; 14289 MW; 0E1E05BCDB7620A9 CRC64;
MLSGRLVLGL VSMAGRVCLC QGSAGSGAIG PVEAAIRTKL EEALSPEVLE LRNESGGHAV
PPGSETHFRV AVVSSRFEGL SPLQRHRLVH AALAEELGGP VHALAIQART PAQWRENSQL
DTSPPCLGGN KKTLGTP
